Purification, nanocrystallization and preliminary X-ray analysis of a C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans

被引:4
作者
Ding, HT
Qiu, SH
Bunzel, RJ
Luo, DL
Arabashi, A
Lu, SY
Symersky, J
Nagy, LA
DeLucas, LJ
Li, SL
Luo, M [1 ]
机构
[1] Peking Univ, Life Sci Coll, Beijing 100871, Peoples R China
[2] Univ Alabama Birmingham, Ctr Biophys Sci & Engn, Birmingham, AL 35294 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词
D O I
10.1107/S0907444903008217
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The C-terminal part of tropomodulin protein 1, isoform A, from Caenorhabditis elegans was expressed in Escherichia coli and purified to homogeneity. Optimized from the initial nanoscreen, crystals grew to dimensions of 0.25 x 0.15 x 0.15 mm at 277 K using 28.0%(v/v) PEG 400 as the precipitant by the hanging-drop vapor-diffusion technique. A data set of 94.9% completeness was collected to a resolution of 1.98 Angstrom at 100 K using a synchrotron X-ray source (SER-CAT). The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a=31.7, b=50.6, c=107.1 Angstrom, and contained one molecule per asymmetric unit.
引用
收藏
页码:1106 / 1108
页数:3
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